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Volumn 287, Issue 28, 2012, Pages 23911-23922

A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast

Author keywords

[No Author keywords available]

Indexed keywords

AZETIDINES; FEEDBACK REGULATION; GELDANAMYCIN; LIGASES; MISFOLDED PROTEINS; MOLECULAR CHAPERONES; PROTEASOMES; PROTEIN AGGREGATES; PROTEIN KINASE; UBIQUITIN; UBIQUITIN LIGASES; UP-REGULATION; WILD-TYPE CELLS; YEAST STRAIN;

EID: 84863615329     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.341164     Document Type: Article
Times cited : (56)

References (50)
  • 1
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F. U., Bracher, A., and Hayer-Hartl, M. (2011) Molecular chaperones in protein folding and proteostasis. Nature 475, 324-332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 2
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers, J., Mogk, A., and Bukau, B. (2010) Cellular strategies for controlling protein aggregation. Nature Rev. Mol. Cell Biol. 11, 777-788
    • (2010) Nature Rev. Mol. Cell Biol. , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 3
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • DOI 10.1083/jcb.143.7.1883
    • Johnston, J. A., Ward, C. L., and Kopito, R. R. (1998) Aggresomes. A cellular response to misfolded proteins. J. Cell Biol. 143, 1883-1898 (Pubitemid 29022611)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 4
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D., Kopito, R., and Frydman, J. (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454, 1088-1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 5
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • Specht, S., Miller, S. B., Mogk, A., and Bukau, B. (2011) Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae. J. Cell Biol. 195, 617-629
    • (2011) J. Cell Biol. , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.2    Mogk, A.3    Bukau, B.4
  • 6
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time. Endoplasmic reticulum-associated degradation
    • Vembar, S. S., and Brodsky, J. L. (2008) One step at a time. Endoplasmic reticulum-associated degradation. Nat. Rev. Mol. Cell Biol. 9, 944-957
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 7
    • 0035146685 scopus 로고    scopus 로고
    • The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
    • DOI 10.1038/35050618
    • Connell, P., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., and Patterson, C. (2001) The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins. Nat. Cell Biol. 3, 93-96 (Pubitemid 32114838)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 93-96
    • Connell, P.1    Ballinger, C.A.2    Jiang, J.3    Wu, Y.4    Thompson, L.J.5    Hohfeld, J.6    Patterson, C.7
  • 8
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • DOI 10.1038/35050509
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., and Cyr, D. M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 3, 100-105 (Pubitemid 32114840)
    • (2001) Nature Cell Biology , vol.3 , Issue.1 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 9
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • Bengtson, M. H., and Joazeiro, C. A. (2010) Role of a ribosome-associated E3 ubiquitin ligase in protein quality control. Nature 467, 470-473
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 11
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E. S., Ma, P. C., Ota, I. M., and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 12
    • 57049182407 scopus 로고    scopus 로고
    • Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
    • Eisele, F., and Wolf, D. H. (2008) Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1. FEBS Lett. 582, 4143-4146
    • (2008) FEBS Lett. , vol.582 , pp. 4143-4146
    • Eisele, F.1    Wolf, D.H.2
  • 13
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J. W., Cheung, S. K., and Hampton, R. Y. (2010) Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. U.S.A. 107, 1106-1111
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 15
    • 80455122748 scopus 로고    scopus 로고
    • Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins
    • Fang, N. N., Ng, A. H., Measday, V., and Mayor, T. (2011) Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat. Cell Biol. 13, 1344-1352
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1344-1352
    • Fang, N.N.1    Ng, A.H.2    Measday, V.3    Mayor, T.4
  • 16
    • 57749116223 scopus 로고    scopus 로고
    • Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery
    • Metzger, M. B., Maurer, M. J., Dancy, B. M., and Michaelis, S. (2008) Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J. Biol. Chem. 283, 32302-32316
    • (2008) J. Biol. Chem. , vol.283 , pp. 32302-32316
    • Metzger, M.B.1    Maurer, M.J.2    Dancy, B.M.3    Michaelis, S.4
  • 17
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTRδF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • DOI 10.1083/jcb.200410065
    • Younger, J. M., Ren, H. Y., Chen, L., Fan, C. Y., Fields, A., Patterson, C., and Cyr, D. M. (2004) A foldable CFTRδF508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase. J. Cell Biol. 167, 1075-1085 (Pubitemid 40066623)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.-Y.2    Chen, L.3    Fan, C.-Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 18
    • 77954178073 scopus 로고    scopus 로고
    • A nucleus-based quality control mechanism for cytosolic proteins
    • Prasad, R., Kawaguchi, S., and Ng, D. T. (2010) A nucleus-based quality control mechanism for cytosolic proteins. Mol. Biol. Cell 21, 2117-2127
    • (2010) Mol. Biol. Cell , vol.21 , pp. 2117-2127
    • Prasad, R.1    Kawaguchi, S.2    Ng, D.T.3
  • 20
    • 84857060671 scopus 로고    scopus 로고
    • Quality control and fate determination of Hsp90 client proteins
    • Theodoraki, M. A., and Caplan, A. J. (2012) Quality control and fate determination of Hsp90 client proteins. Biochim. Biophys. Acta 1823, 683-688
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 683-688
    • Theodoraki, M.A.1    Caplan, A.J.2
  • 21
    • 81355127301 scopus 로고    scopus 로고
    • UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition
    • Sultana, R., Theodoraki, M. A., and Caplan, A. J. (2012) UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition. Exp. Cell Res. 318, 53-60
    • (2012) Exp. Cell Res. , vol.318 , pp. 53-60
    • Sultana, R.1    Theodoraki, M.A.2    Caplan, A.J.3
  • 22
    • 77951757948 scopus 로고    scopus 로고
    • ErbB2 trafficking and degradation associated with K48 and K63 polyubiquitination
    • Marx, C., Held, J. M., Gibson, B. W., and Benz, C. C. (2010) ErbB2 trafficking and degradation associated with K48 and K63 polyubiquitination. Cancer research 70, 3709-3717
    • (2010) Cancer Research , vol.70 , pp. 3709-3717
    • Marx, C.1    Held, J.M.2    Gibson, B.W.3    Benz, C.C.4
  • 23
  • 24
    • 64049090940 scopus 로고    scopus 로고
    • Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins
    • Metzger, M. B., and Michaelis, S. (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol. Biol. Cell 20, 1006-1019
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1006-1019
    • Metzger, M.B.1    Michaelis, S.2
  • 25
    • 33644843117 scopus 로고    scopus 로고
    • A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor
    • DOI 10.1111/j.1365-2958.2006.05097.x
    • Hahn, J. S., Neef, D. W., and Thiele, D. J. (2006) A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Mol. Microbiol. 60, 240-251 (Pubitemid 43363302)
    • (2006) Molecular Microbiology , vol.60 , Issue.1 , pp. 240-251
    • Hahn, J.-S.1    Neef, D.W.2    Thiele, D.J.3
  • 26
    • 11244343965 scopus 로고    scopus 로고
    • Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase
    • DOI 10.1074/jbc.M410085200
    • Wang, L., Mao, X., Ju, D., and Xie, Y. (2004) Rpn4 is a physiological substrate of the Ubr2 ubiquitin ligase. J. Biol. Chem. 279, 55218-55223 (Pubitemid 40066517)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55218-55223
    • Wang, L.1    Mao, X.2    Ju, D.3    Xie, Y.4
  • 27
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • DOI 10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2- 2
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C. A useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132 (Pubitemid 28062863)
    • (1998) Yeast , vol.14 , Issue.2 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 29
    • 35248818750 scopus 로고    scopus 로고
    • Akt shows variable sensitivity to an Hsp90 inhibitor depending on cell context
    • DOI 10.1016/j.yexcr.2007.06.022, PII S0014482707003151
    • Theodoraki, M. A., Kunjappu, M., Sternberg, D. W., and Caplan, A. J. (2007) Akt shows variable sensitivity to an Hsp90 inhibitor depending on cell context. Exp. Cell Res. 313, 3851-3858 (Pubitemid 47561893)
    • (2007) Experimental Cell Research , vol.313 , Issue.18 , pp. 3851-3858
    • Theodoraki, M.A.1    Kunjappu, M.2    Sternberg, D.W.3    Caplan, A.J.4
  • 30
    • 0025362399 scopus 로고
    • A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae
    • Schmitt, M. E., Brown, T. A., and Trumpower, B. L. (1990) A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucleic Acids Res. 18, 3091-3092 (Pubitemid 20178191)
    • (1990) Nucleic Acids Research , vol.18 , Issue.10 , pp. 3091-3092
    • Schmitt, M.E.1    Brown, T.A.2    Trumpower, B.L.3
  • 32
    • 59449095866 scopus 로고    scopus 로고
    • Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins
    • Flom, G. A., Lemieszek, M., Fortunato, E. A., and Johnson, J. L. (2008) Farnesylation of Ydj1 is required for in vivo interaction with Hsp90 client proteins. Mol. Biol. Cell 19, 5249-5258
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5249-5258
    • Flom, G.A.1    Lemieszek, M.2    Fortunato, E.A.3    Johnson, J.L.4
  • 33
    • 83755178155 scopus 로고    scopus 로고
    • The [RNQ+] prion. A model of both functional and pathological amyloid
    • Stein, K. C., and True, H. L. (2011) The [RNQ+] prion. A model of both functional and pathological amyloid. Prion 5, 291-298
    • (2011) Prion , vol.5 , pp. 291-298
    • Stein, K.C.1    True, H.L.2
  • 34
    • 0037053566 scopus 로고    scopus 로고
    • Huntingtin toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • DOI 10.1083/jcb.200112104
    • Meriin, A. B., Zhang, X., He, X., Newnam, G. P., Chernoff, Y. O., and Sherman, M. Y. (2002) Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 157, 997-1004 (Pubitemid 34839774)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 35
    • 0033485869 scopus 로고    scopus 로고
    • The E2-E3 interaction in the N-end rule pathway. The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain
    • Xie, Y., and Varshavsky, A. (1999) The E2-E3 interaction in the N-end rule pathway. The RING-H2 finger of E3 is required for the synthesis of multiubiquitin chain. EMBO J. 18, 6832-6844
    • (1999) EMBO J. , vol.18 , pp. 6832-6844
    • Xie, Y.1    Varshavsky, A.2
  • 38
    • 78649894111 scopus 로고    scopus 로고
    • The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases
    • Hwang, C. S., Shemorry, A., Auerbach, D., and Varshavsky, A. (2010) The N-end rule pathway is mediated by a complex of the RING-type Ubr1 and HECT-type Ufd4 ubiquitin ligases. Nat. Cell Biol. 12, 1177-1185
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1177-1185
    • Hwang, C.S.1    Shemorry, A.2    Auerbach, D.3    Varshavsky, A.4
  • 39
    • 0026362366 scopus 로고
    • Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability
    • Seufert, W., and Jentsch, S. (1991) Yeast ubiquitin-conjugating enzymes involved in selective protein degradation are essential for cell viability. Acta Biol. Hung. 42, 27-37
    • (1991) Acta Biol. Hung. , vol.42 , pp. 27-37
    • Seufert, W.1    Jentsch, S.2
  • 40
    • 80053564708 scopus 로고    scopus 로고
    • Amyloid in neurodegenerative diseases. Friend or foe?
    • Wolfe, K. J., and Cyr, D. M. (2011) Amyloid in neurodegenerative diseases. Friend or foe? Semin. Cell Dev. Biol. 22, 476-481
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 476-481
    • Wolfe, K.J.1    Cyr, D.M.2
  • 42
    • 0346736509 scopus 로고    scopus 로고
    • Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M204686200
    • Trotter, E. W., Kao, C. M., Berenfeld, L., Botstein, D., Petsko, G. A., and Gray, J. V. (2002) Misfolded proteins are competent to mediate a subset of the responses to heat shock in Saccharomyces cerevisiae. J. Biol. Chem. 277, 44817-44825 (Pubitemid 36159076)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 44817-44825
    • Trotter, E.W.1    Kao, C.M.-F.2    Berenfeld, L.3    Botstein, D.4    Petsko, G.A.5    Gray, J.V.6
  • 43
    • 2942620845 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome
    • DOI 10.1016/j.febslet.2004.04.078, PII S001457930400554X
    • London, M. K., Keck, B. I., Ramos, P. C., and Dohmen, R. J. (2004) Regulatory mechanisms controlling biogenesis of ubiquitin and the proteasome. FEBS Lett. 567, 259-264 (Pubitemid 38748402)
    • (2004) FEBS Letters , vol.567 , Issue.2-3 , pp. 259-264
    • London, M.K.1    Keck, B.I.2    Ramos, P.C.3    Dohmen, R.J.4
  • 44
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • DOI 10.1016/S0092-8674(00)81223-4
    • Glover, J. R., and Lindquist, S. (1998) Hsp104, Hsp70, and Hsp40. A novel chaperone system that rescues previously aggregated proteins. Cell 94,73-82 (Pubitemid 28347471)
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 45
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin, V., McEwan, D. G., Novak, I., and Dikic, I. (2009) A role for ubiquitin in selective autophagy. Mol. Cell 34, 259-269
    • (2009) Mol. Cell , vol.34 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 46
    • 34347392289 scopus 로고    scopus 로고
    • The structure and function of Saccharomyces cerevisiae proteinase A
    • DOI 10.1002/yea.1485
    • Parr, C. L., Keates, R. A., Bryksa, B. C., Ogawa, M., and Yada, R. Y. (2007) The structure and function of Saccharomyces cerevisiae proteinase A. Yeast 24, 467-480 (Pubitemid 47019038)
    • (2007) Yeast , vol.24 , Issue.6 , pp. 467-480
    • Parr, C.L.1    Keates, R.A.B.2    Bryksa, B.C.3    Ogawa, M.4    Yada, R.Y.5
  • 48
    • 78751554804 scopus 로고    scopus 로고
    • The tumor suppressor protein menin inhibits AKT activation by regulating its cellular localization
    • Wang, Y., Ozawa, A., Zaman, S., Prasad, N. B., Chandrasekharappa, S. C., Agarwal, S. K., and Marx, S. J. (2011) The tumor suppressor protein menin inhibits AKT activation by regulating its cellular localization. Cancer Res. 71, 371-382
    • (2011) Cancer Res. , vol.71 , pp. 371-382
    • Wang, Y.1    Ozawa, A.2    Zaman, S.3    Prasad, N.B.4    Chandrasekharappa, S.C.5    Agarwal, S.K.6    Marx, S.J.7
  • 49
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of Longevity in Caenorhabditis elegans by Heat Shock Factor and Molecular Chaperones
    • DOI 10.1091/mbc.E03-07-0532
    • Morley, J. F., and Morimoto, R. I. (2004) Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol. Biol. Cell 15, 657-664 (Pubitemid 38146482)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.2 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 50
    • 11144352246 scopus 로고    scopus 로고
    • Pheromone-dependent destruction of the Tec1 transcription factor is required for MAP kinase signaling specificity in yeast
    • DOI 10.1016/j.cell.2004.11.052, PII S0092867404011651
    • Bao, M. Z., Schwartz, M. A., Cantin, G. T., Yates, J. R., 3rd, and Madhani, H. D. (2004) Pheromone-dependent destruction of the Tec1 transcription factor is required for MAP kinase signaling specificity in yeast. Cell 119, 991-1000 (Pubitemid 40037612)
    • (2004) Cell , vol.119 , Issue.7 , pp. 991-1000
    • Bao, M.Z.1    Schwartz, M.A.2    Cantin, G.T.3    Yates III, J.R.4    Madhani, H.D.5


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